zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
4-389
0e+00
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.
The actual alignment was detected with superfamily member NF038288:
Pssm-ID: 468453 [Multi-domain] Cd Length: 390 Bit Score: 564.79 E-value: 0e+00
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
4-389
0e+00
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.
Pssm-ID: 468453 [Multi-domain] Cd Length: 390 Bit Score: 564.79 E-value: 0e+00
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
5-225
5.91e-91
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.
Pssm-ID: 349766 Cd Length: 198 Bit Score: 272.09 E-value: 5.91e-91
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
5-210
4.33e-68
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.
Pssm-ID: 396860 Cd Length: 179 Bit Score: 212.88 E-value: 4.33e-68
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
3-337
1.81e-45
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274151 [Multi-domain] Cd Length: 341 Bit Score: 159.53 E-value: 1.81e-45
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
256-371
1.13e-37
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.
Pssm-ID: 214844 [Multi-domain] Cd Length: 92 Bit Score: 131.18 E-value: 1.13e-37
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
4-389
0e+00
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.
Pssm-ID: 468453 [Multi-domain] Cd Length: 390 Bit Score: 564.79 E-value: 0e+00
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
5-225
5.91e-91
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.
Pssm-ID: 349766 Cd Length: 198 Bit Score: 272.09 E-value: 5.91e-91
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
5-210
4.33e-68
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.
Pssm-ID: 396860 Cd Length: 179 Bit Score: 212.88 E-value: 4.33e-68
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
3-337
1.81e-45
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274151 [Multi-domain] Cd Length: 341 Bit Score: 159.53 E-value: 1.81e-45
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
256-371
1.13e-37
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.
Pssm-ID: 214844 [Multi-domain] Cd Length: 92 Bit Score: 131.18 E-value: 1.13e-37
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
256-371
4.13e-26
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of putative metal chaperones that can be separated into up to 15 subgroups. In addition to known roles in cobalamin biosynthesis and the activation of the Fe-type nitrile hydratase, this family is also known to be involved in the response to zinc limitation. The CobW subgroup involved in cobalamin synthesis represents only a small sub-fraction of the family.
Pssm-ID: 462228 [Multi-domain] Cd Length: 93 Bit Score: 100.39 E-value: 4.13e-26
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
14-212
5.82e-05
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases.
Pssm-ID: 349775 Cd Length: 203 Bit Score: 43.74 E-value: 5.82e-05
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ...
1-244
9.22e-04
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; This family contains Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins. Shulin is a negative regulator of the ciliary outer dynein arm (ODA). It binds newly synthesized ODAs, locks the dynein motors together by shutting off motor activity, and facilitates the delivery of ODAs from the cytoplasm to their final position in the cilia. ODAs, together with inner dynein arms (IDAs), are arrayed along a microtubule-based structure called the axoneme and drive the movement of cilia. Human C20orf194 interacts with the small GTPase Arf-like 3 (ARL3) and may act as its effector. The rs6051702 single nucleotide polymorphism (SNP) within the C20orf194 gene is associated with inosine triphosphatase (ITPA) functional gene polymorphisms that were found to influence RBV-induced hemoglobin (Hb)-decline during treatment of chronic hepatitis C patients with pegylated interferon (PEG-IFN) plus ribavirin (RBV).
Pssm-ID: 438574 [Multi-domain] Cd Length: 1092 Bit Score: 41.57 E-value: 9.22e-04
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress ...
178-223
5.28e-03
Obg GTPase; The Obg nucleotide binding protein subfamily has been implicated in stress response, chromosome partitioning, replication initiation, mycelium development, and sporulation. Obg proteins are among a large group of GTP binding proteins conserved from bacteria to humans. The E. coli homolog, ObgE is believed to function in ribosomal biogenesis. Members of the subfamily contain two equally and highly conserved domains, a C-terminal GTP binding domain and an N-terminal glycine-rich domain.
Pssm-ID: 206685 [Multi-domain] Cd Length: 170 Bit Score: 37.40 E-value: 5.28e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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